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(Received for publication, April 11, 1997, and in revised form, April 28, 1997)
From the Department of Pathology, Robert Wood Johnson Medical
School, Piscataway, New Jersey 08854
Laminin-2, a heterotrimer composed of
Volume 272, Number 46,
Issue of November 14, 1997
pp. 29330-29336
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
The Laminin
2-Chain Short Arm Mediates Cell Adhesion through
Both the 1
1 and 21 Integrins
2, 
1,
and 
1 subunits, is the primary laminin isoform found in muscle and
peripheral nerve and is essential for the development and stability of
basement membranes in these tissues. Expression of a domain
VI-truncated laminin 2-chain results in muscle degeneration and
peripheral nerve dysmyelination in the dy2J
dystrophic mouse. We have expressed amino-terminal domains VI through
IVb of the laminin 2-chain, as well as its laminin-1 1-chain
counterpart, to identify candidate cell-interactive functions of this
critical region. Using integrin-specific antibodies, recognition sites
for the 11 and 21 integrins were identified in the short arms of both laminin 1- and 2-chain isoforms. Comparisons with a
- chimeric short arm protein possessing 1-chain domain VI further localized these activities to -chain domain VI. In addition, we found that the laminin 2-chain short arm supported neurite outgrowth independent of other laminin-2 subunits. A heparin/heparan sulfate binding activity was also localized to this region of the
laminin 2 subunit. These data provide the first evidence that domain
VI of the laminin 2-chain mediates interactions with cell surface
receptors and suggest that these integrin and heparin binding sites,
alone or in concert, may play an important role in muscle and
peripheral nerve function.
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